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Glutathione Peroxidase from bovine erythrocytes

lyophilized powder, ≥300 units/mg protein

GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:


lyophilized powder

Quality Level

specific activity

≥300 units/mg protein

mol wt

84.5 kDa


Protein, 10-30% modified Warburg-Christian

shipped in

dry ice

storage temp.


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General description

Glutathione peroxidase is an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of human endometrium.


Glutathione peroxidase from bovine erythrocytes was used as a positive control in cloning and characterization of full-length cDNAs encoding two glutathione peroxidases (GpXs) from Globodera rostochiensis. It was used for the determination of glutathione peroxidase activity in human milk.
Glutathione Peroxidase from bovine erythrocytes has been used as an oxygen radical scavenger to study its effect on cytotoxicity of 1,3-dilinoleoylglycerol (DLG) against E1A-3Y1 cells.


100, 200, 500 units in serum bottle

Biochem/physiol Actions

Glutathione peroxidase helps to reduce (peroxides) H2O2 to water and lipid peroxides to lipid alcohols.
Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown.
Protects cells against oxidative damage by catalyzing the reduction of hydrogen peroxide in the presence of reducing agent glutathione. In cellular membranes it may induce lipid peroxidation through the reduction of hydrogen peroxide or polyunsaturated fatty acid hydroperoxides.

Unit Definition

One unit will catalyze the oxidation by H2O2 of 1.0 μmole of reduced glutathione to oxidized glutathione per min at pH 7.0 at 25 °C.

Physical form

Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts

Other Notes

Note: At the reported pH optimum of 8.8, we have found the activity to be approx. 10 times that at pH 7.0. However, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of GSH, our unit is defined at pH 7.0.


Health hazard

Signal Word


Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

J T Jones et al.
Gene, 324, 47-54 (2003-12-25)
We report the cloning and characterisation of full-length DNAs complementary to RNA (cDNAs) encoding two glutathione peroxidases (GpXs) from a plant parasitic nematode, the potato cyst nematode (PCN) Globodera rostochiensis. One protein has a functional signal peptide that targets the
The role of oxidative stress in endometriosis
Handbook of Fertility, 273-281 (2015)
Angeles Torres et al.
Die Nahrung, 47(6), 430-433 (2004-01-20)
An analytical method for determining glutathione peroxidase (GPx) (EC activity in whole blood has been adapted to human milk samples. The values obtained for precision (relative standard deviation: 8.4%), linearity and accuracy (recovery: 90.4%) indicate the adequacy of the
Reactive oxygen species, oxidative stress, and vascular biology in hypertension
Comprehensive hypertension, 337-344 (2007)
Yue Wang et al.
Analytical chemistry, 92(2), 1997-2004 (2019-12-21)
Solid evidence confirms that glutathione peroxidase (GPx) is a kind of vital protease in the first-line antioxidant defense system and participates in regulation of redox homeostasis as well as the pentose phosphate pathway. However, the current methods cannot achieve real-time

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